{Reference Type}: Journal Article
{Author}: Papp, V.; Geoesel, A.; Eros-Honti, Zs.
{Year}: 2012
{Title}: NATIVE GANODERMA SPECIES FROM THE CARPATHIAN BASIN WITH THE PERSPECTIVE OF CULTIVATION REVIEW
{Tag}: 0
{Star}: 0
{Journal}: ACTA ALIMENTARIA
{Volume}: 41
{Pages}: 160-170
{ISBN/ISSN}: 0139-3006
{Keywords}: MUSHROOM-FORMING FUNGI; ANTIMICROBIAL ACTIVITIES; LUCIDUM COMPLEX; FRUIT BODIES; OIL PALM; APPLANATUM; TAXONOMY; EXOPOLYSACCHARIDE; CONSTITUENTS; RESINACEUM; Central-Europe; medicinal mushroom; taxonomy; Ganoderma
{Abstract}: Ganoderma is a worldwide distributed genus of polyporoid fungi causing white-rot. The sporocarps of these species are popular drug in the traditional medicine of the Far East. Although several species are proven to contain chemicals of different biological activities, only Ganoderma lucidum is cultivated on the large scale. It is an important goal of mushroom growing to involve genetically diverse strains in this field of industry (e. g. for Agaricus, Pleurotus), thus the range of cultivated Ganoderma species should also be broadened in the future. Within the Carpathian Basin, we have the possibility to isolate strains from 6 species beside G. lucidum: G. adspersum, G. applanatum (syn. G. lipsiense), G. carnosum (syn. G. atkinsonii), G. cupreolaccatum (G. pfeifferi), G. resinaceum and G. valesiacum. In the present review, by describing the taxonomical status and the ecological characteristic of the species, we depict the biological background of the medicinal potential, as well as the cultivation possibilities (both sporocarp production and liquid mycelia cultures) of these species.
{Author Address}: Corvinus Univ Budapest, Dept Bot, H-1118 Budapest, Hungary; Corvinus Univ Budapest, Soroksar Bot Garden, H-1118 Budapest, Hungary; Corvinus Univ Budapest, Dept Vegetable & Mushroom Growing, H-1118 Budapest, Hungary; Corvinus Univ Budapest, Dept Bot, H-1118 Budapest, Hungary; Corvinus Univ Budapest, Soroksar Bot Garden, H-1118 Budapest, Hungary
{Database Provider}: Web of Science SCI
{Language}: English
{Country}: Hungary; Hungary; Hungary

{Reference Type}: Journal Article
{Author}: Tian, G. T.; Zhang, G. Q.; Wang, H. X.; Ng, T. B.
{Year}: 2012
{Title}: Purification and characterization of a novel laccase from the mushroom Pleurotus   nebrodensis
{URL}: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=22946027&query_hl=1
{Tag}: 0
{Star}: 0
{Journal}: Acta Biochim Pol
{Volume}: 59
{Issue}: 3
{Pages}: 407-12
{Date Displayed}: 2012
{Date}: 2012-01-20
{Type of Work}: Journal Article; Research Support, Non-U.S. Gov't
{Accession Number}: 22946027
{Keywords}: Adsorption; Amino Acid Sequence; Catechols/chemistry; Chromatography, DEAE-Cellulose/methods; Chromatography, Gel/methods; Electrophoresis, Polyacrylamide Gel/methods; Enzyme Activation; Enzyme Assays/methods; Fruiting Bodies, Fungal/enzymology; Fungal Proteins/chemistry/*isolation & purification; Hydrogen-Ion Concentration; Laccase/chemistry/*isolation & purification; Molecular Weight; Phenylenediamines/chemistry; Pleurotus/*enzymology; Pyrogallol/chemistry; Sequence Analysis, Protein/methods; Substrate Specificity; Temperature
{Abstract}: A novel laccase with a molecular mass of 64 kDa and the N-terminal sequence AIGPDDTINF was isolated from fresh fruiting bodies of the mushroom Pleurotus nebrodensis. The purification protocol comprised ion exchange chromatography on DEAE-cellulose, CM-cellulose, and Q-Sepharose, and gel filtration on Superdex 75. The laccase was adsorbed on DEAE-cellulose and Q-Sepharose, but not on CM-cellulose. It demonstrated an optimal temperature of 70 degrees C. The enzyme   activity increased steadily over the temperature range 20 degrees C-70 degrees C. There was only a slight reduction in activity at 80 degrees C. However, all activity disappeared following exposure to 100 degrees C for 10 minutes. The enzyme activity changed only slightly over the pH range 3-5, with the optimum at   pH 5, but underwent a precipitous decline when the pH was elevated to 6, and was   undetectable at pH 8 and pH 9.
{Author Address}: Institute of Biotechnology and Germplasmic Resource, Yunnan Academy of Agricultural Science, Kunming, China.
{Language}: eng

{Reference Type}: Journal Article
{Author}: Sun, J.; Zhao, Y.; Chai, H.; Wang, H.; Ng, T. B.
{Year}: 2011
{Title}: A novel alkaline protease with antiproliferative activity from fresh fruiting bodies of the toxic wild mushroom Amanita farinosa
{URL}: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=22146135&query_hl=1
{Tag}: 0
{Star}: 0
{Journal}: Acta Biochim Pol
{Volume}: 58
{Issue}: 4
{Pages}: 567-72
{Date Displayed}: 2011
{Date}: 2011-01-20
{Type of Work}: Journal Article; Research Support, Non-U.S. Gov't
{Accession Number}: 22146135
{Keywords}: Adsorption; Amanita/*enzymology; Amino Acid Sequence; Antineoplastic Agents, Phytogenic/chemistry/*isolation &
           purification/pharmacology; Cell Proliferation/drug effects; Cell Survival; Chromatography, Affinity; Chromatography, Gel; Chromatography, Ion Exchange/methods; Electrophoresis, Polyacrylamide Gel; Enzyme Activation; Enzyme Assays; Fruiting Bodies, Fungal/*enzymology; Fungal Proteins/chemistry/isolation & purification/pharmacology; Hep G2 Cells; Humans; Hydrogen-Ion Concentration; Peptide Hydrolases/chemistry/*isolation & purification/pharmacology; Temperature
{Abstract}: A novel protease with a molecular mass of 15 kDa was purified from fresh fruiting bodies of the wild mushroom Amanita farinosa. The purification protocol entailed   anion exchange chromatography on DEAE-cellulose, affinity chromatography on Affi-gel blue gel, cation exchange chromatography on SP-Sepharose, and gel filtration by fast protein liquid chromatography on Superdex 75. The protease was unadsorbed on DEAE-cellulose but adsorbed on Affi-gel blue gel and SP-Sepharose.   It demonstrated a single 15-kDa band in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS/PAGE) and a 15-kDa peak in gel filtration. The optimal pH and optimal temperature of the protease were pH 8.0 and 65 degrees C, respectively. Proliferation of human hepatoma HepG2 cells was inhibited by the protease with an IC(50) of 25 microM. The protease did not have antifungal or ribonuclease activity.
{Author Address}: State Key Laboratory for Agrobiotechnology and Department of Microbiology, China   Agricultural University, Beijing, China.
{Language}: eng

{Reference Type}: Journal Article
{Author}: Grodecka, M.; Czerwinski, M.; Duk, M.; Lisowska, E.; Wasniowska, K.
{Year}: 2010
{Title}: Analysis of recombinant Duffy protein-linked N-glycans using lectins and glycosidases
{URL}: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=20234884&query_hl=1
{Tag}: 0
{Star}: 0
{Journal}: Acta Biochim Pol
{Volume}: 57
{Issue}: 1
{Pages}: 49-53
{Date Displayed}: 2010
{Date}: 2010-01-20
{Type of Work}: Journal Article; Research Support, Non-U.S. Gov't
{Accession Number}: 20234884
{Keywords}: Ascomycota/metabolism; Duffy Blood-Group System/*analysis/metabolism; Glycoside Hydrolases/*metabolism; Humans; K562 Cells; Lectins/*metabolism; Plant Lectins/*metabolism; Plants/metabolism; Polysaccharides/*metabolism; Protein Binding; Receptors, Cell Surface/*analysis/metabolism; Recombinant Proteins/analysis/metabolism
{Abstract}: Duffy antigen is a glycosylated blood group protein acting as a malarial and chemokine receptor. Using glycosylation mutants we have previously demonstrated,   that all three potential glycosylation sites of the Duffy antigen are occupied by N-linked oligosaccharide chains. In this study, wild-type Duffy glycoprotein and   three mutants, each containing a single N-glycan, were used to characterize the oligosaccharide chains by lectin blotting and endoglycosidase digestion. The positive reaction of all the recombinant Duffy forms with Datura stramonium and Sambucus nigra lectins showed that each Duffy N-linked glycan contains Galbeta1-4GlcNAc units terminated by (alpha2-6)-linked sialic acid residues, typical of complex oligosaccharides. The reactivity with Aleuria aurantia and Lens culinaris lectins suggested the presence of (alpha1-6)-linked fucose at the   N-glycan chitobiose core. The failure of the Galanthus nivalis and Canavalia ensiformis lectins to bind to any of the Duffy mutants or to the wild-type antigen indicated that none of the three Duffy N-glycosylation sites carries detectable levels of high-mannose oligosaccharide chains. Digestion of Duffy samples with peptide N-glycosidase F and endoglycosidase H confirmed the presence of N-linked complex oligosaccharides. Our results indicate that Duffy antigen N-glycans are mostly core-fucosylated complex type oligosaccharides rich in N-acetyllactosamine and terminated by (alpha2-6)-linked sialic acid residues.
{Author Address}: Department of Immunochemistry, Ludwik Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, Wroclaw, Poland.
{Language}: eng